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|Title:||Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor||Authors:||Yap, Lijian
Noble, Christian G.
Lim, Siew Pheng
Liew, Chong Wai
|Keywords:||DRNTU::Science::Biological sciences::Microbiology::Virology||Issue Date:||2013||Source:||Noble, C. G., Lim, S. P., Chen, Y.-L., Liew, C. W., Yap, L., Lescar, J., et al. (2013). Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor. Journal of virology, 87(9), 5291-5295.||Series/Report no.:||Journal of virology||Abstract:||We report a highly reproducible method to crystallize the RNA-dependent RNA polymerase (RdRp) domain of dengue virus serotype 3 (DENV-3), allowing structure refinement to a 1.79-Å resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor cocrystal structure at a 2.1-Å resolution. The inhibitor binds to the RdRp as a dimer and causes conformational changes in the protein. The improved crystallization conditions and new structural information should accelerate structure-based drug discovery.||URI:||https://hdl.handle.net/10356/103700
|ISSN:||0022-538X||DOI:||10.1128/JVI.00045-13||Rights:||© 2013 American Society for Microbiology (ASM). This paper was published in Journal of Virology and is made available as an electronic reprint (preprint) with permission of American Society for Microbiology (ASM). The paper can be found at the following official DOI: [http://dx.doi.org/10.1128/JVI.00045-13]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
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